2bfk: Difference between revisions

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{{Seed}}
[[Image:2bfk.png|left|200px]]
[[Image:2bfk.png|left|200px]]


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==About this Structure==
==About this Structure==
2BFK is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFK OCA].  
[[2bfk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFK OCA].  


==Reference==
==Reference==
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[[Category: Metallo-beta-lactamase]]
[[Category: Metallo-beta-lactamase]]
[[Category: Zinc]]
[[Category: Zinc]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep  3 16:23:29 2009''

Revision as of 00:11, 15 March 2011

File:2bfk.png

Template:STRUCTURE 2bfk

BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH7 USING 20MM ZNSO4 IN BUFFER. 1MM DTT WAS USED AS A REDUCING AGENTBACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH7 USING 20MM ZNSO4 IN BUFFER. 1MM DTT WAS USED AS A REDUCING AGENT

Template:ABSTRACT PUBMED 15779910

About this StructureAbout this Structure

2bfk is a 2 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2][xtra 3]

  1. Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM. Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism. Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:15779910 doi:10.1021/bi047709t
  2. Rasia RM, Vila AJ. Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-beta-lactamase. Biochemistry. 2002 Feb 12;41(6):1853-60. PMID:11827530
  3. Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ. Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry. 1998 Sep 8;37(36):12404-11. PMID:9730812 doi:http://dx.doi.org/10.1021/bi980506i

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